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systemic lupus erythematosus patients with low plasma ficolin-2 levels had an increased risk of having lupus nephritis
Ficolin-2 protein could bind with HIV-1 envelope glycoprotein (show ERVW-1 Proteins) gp120 (show ITIH4 Proteins), and subsequently induce complement dependent cytotoxicity.
The FCN2 c.772G>T genotype appears to be associated with predisposition to chronic adenotonsillitis in the pediatric age group.
Serum levels of ficolin-2 and ficolin-3 (show FCN3 Proteins) were significantly lower in the cardiac syndrome X patients compared to controls.
association of FCN2 polymorphisms with nephritis and severe cumulative damage in SLE patients; no association with rheumatoid arthritis development
-557 A>G, -64 A>C and +6424 G>T SNPs of the FCN2 gene were correlated with pulmonary TB.
FCN2 and MBL2 (show MBL2 Proteins) allele frequencies were similarly distributed in early and late age-related macular degeneration cases compared with controls
this study provide novel insight in the binding and complement activating capacity of the lectin pathway initiation molecules ficolin-2 and ficolin-3 (show FCN3 Proteins) towards relevant Gram-negative pathogens of pathophysiological relevance.
Findings indicate the FCN2 variant +6359C>T is associated with the occurrence of visceral leishmaniasis and that ficolin-2 serum levels are elevated in Leishmania infections.
L-ficolin modulates the immune response to A. fumigatus.
Ficolin-2 defends against virulent Mycobacteria tuberculosis infection in vivo, and its insufficiency is associated with infection in humans.
Data show that ficolin-B is stored in and set free from immature granulocytic myeloid cells indicating a role in the early infection-induced cellular response of these inflammatory cells.
FcnA-deficient and FcnA/ficolin B double-deficient mice lack FcnA-mediated complement activation in the sera, because of absence of complexes comprising FcnA and MBL-associated serine proteases.
These results identify mouse ficolin-B as a functional member of the ficolin family activating complement via the lectin pathway.
Results show that ficolin B in mouse bone marrow is an oligomeric protein. Ficolin B contained very low, but detectable, amounts of MASP-2 and sMAP and showed detectable C4-deposition activity on immobilized N-acetylglucosamine.
Ficolin B exhibited a distinct ontogeny pattern that switched from embryonic liver to postnatal bone marrow and spleen. The cells that express ficolin B mRNA were identified as belonging to the myeloid cell lineage.
Ficolin B showed multimeric structures and revealed binding to both N-acetylglucosamine and N-acetylgalactosamine. Ficolin B specifically recognized sialic acid residues. Ficolin B plays a distinct role through its unique carbohydrate-binding specificity.
The product of this gene belongs to the ficolin family of proteins. This family is characterized by the presence of a leader peptide, a short N-terminal segment, followed by a collagen-like region, and a C-terminal fibrinogen-like domain. This gene is predominantly expressed in the liver, and has been shown to have carbohydrate binding and opsonic activities. Alternatively spliced transcript variants encoding different isoforms have been identified.
ficolin (collagen/fibrinogen domain containing lectin) 2 (hucolin)
, ficolin 2
, 37 kDa elastin-binding protein
, collagen/fibrinogen domain-containing protein 2
, ficolin B
, serum lectin p35